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Protein Preparation, Crystallization and Preliminary X-Ray Crystallographic Studies of Smu.1392c from Streptococcus mutans

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Abstract:

Smu.1392c is a protein with 158 residues of uncharacterized function. Bioinformatics studies predict it is a putative acetyltransferase. In order to identify its exact function via structural studies, Smu.1392c gene was amplified from Streptococcus mutans genomic DNA and cloned into expression vector PET28a. Smu.1392c was crystallized and diffracted to a resolution of 3 Å in-house. The crystal belongs to R32 space group, with unit cell parameters a= b= 229.10, c= 63.49 Å. There are 2 or 3 molecules in the asymmetric unit.





Keywords: Smu.1392c; X-ray diffraction; protein crystallography

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986606778777542

Affiliations: Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Beijing, 100049, China.

Publication date: October 1, 2006

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
ben/ppl/2006/00000013/00000010/art00015
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